From eilatin to isoeilatin: a skeletal rearrangement strongly influences pi-stacking of Ru(II) complex

Elastic fiber contains the protein elastin along with lesser amounts of other proteins and glycoproteins. The main property of elastin is that it will return to its original shape after being stretched or compressed. Elastic fibers are prominent in elastic tissues found in skin and the elastic ligaments of the vertebral column.
Ligaments and tendons are made of dense regular connective tissue, but in ligaments not all fibers are parallel. Dense regular elastic tissue contains elastin fibers and...

Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
Linkage isomers occur when the coordination compound contains a ligand that can bind to the transition metal center through two different atoms. For example, the CN− ligand can bind through the carbon atom or through the nitrogen atom. Similarly, SCN− can be...

Deformation occurs in axial and transverse directions when an axial load is applied to a slender bar. This deformation impacts the cubic element within the bar, transforming it into either a rectangular parallelepiped or a rhombus, contingent on its orientation. This transformation process induces shearing strain. Axial loading elicits both shearing and normal strains. Applying an axial load instigates equal normal and shearing stresses on elements oriented at a 45° angle to the load axis.

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.